Purification, crystallization and preliminary crystallographic analysis of a 6-pyruvoyltetrahydropterin synthase homologue from Esherichia coli
- Division of Applied Life Science, Gyeongsang National University, Jinju 660-711 (Korea, Republic of)
- Mitochondrial Research Group, School of Biotechnology and Biomedical Science, Inje University, Kimhae 621-749 (Korea, Republic of)
The 6-pyruvoyltetrahydropterin synthase from E. coli has been crystallized in two crystal forms. Diffraction data were collected from hexagonal- and rectangular-shaped crystals to 3.0 and 2.3 Å, respectively. 6-Pyruvoyltetrahydropterin synthase from E. coli (ePTPS) has been crystallized using the hanging-drop vapour-diffusion method. Hexagonal- and rectangular-shaped crystals were obtained. Diffraction data were collected from the hexagonal and rectangular crystals to 3.0 and 2.3 Å resolution, respectively. The hexagonal plate-shaped crystals belonged to space group P321, with unit-cell parameters a = b = 112.59, c = 68.82 Å, and contained two molecules in the asymmetric unit. The rectangular crystals belonged to space group I222, with unit-cell parameters a = 112.76, b = 117.66, c = 153.57 Å, and contained six molecules in the asymmetric unit. The structure of ePTPS in both crystal forms has been determined by molecular replacement.
- OSTI ID:
- 22360494
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 2; Other Information: PMCID: PMC2374169; PMID: 18271114; PUBLISHER-ID: en5280; OAI: oai:pubmedcentral.nih.gov:2374169; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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